ID   A0A2T4AJ63_TRIHA        Unreviewed;       366 AA.
AC   A0A2T4AJ63;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=M431DRAFT_493549 {ECO:0000313|EMBL:PTB57072.1};
OS   Trichoderma harzianum CBS 226.95.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB57072.1, ECO:0000313|Proteomes:UP000241690};
RN   [1] {ECO:0000313|EMBL:PTB57072.1, ECO:0000313|Proteomes:UP000241690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB57072.1,
RC   ECO:0000313|Proteomes:UP000241690};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
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DR   EMBL; KZ679678; PTB57072.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4AJ63; -.
DR   STRING; 983964.A0A2T4AJ63; -.
DR   OrthoDB; 2685592at2759; -.
DR   Proteomes; UP000241690; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR47990:SF62; IRON_ASCORBATE OXIDOREDUCTASE DDB_G0283291-RELATED; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|RuleBase:RU003682};
KW   Metal-binding {ECO:0000256|RuleBase:RU003682};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW   Reference proteome {ECO:0000313|Proteomes:UP000241690}.
FT   DOMAIN          178..300
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   366 AA;  40791 MW;  DE139F7F37D56FE6 CRC64;
     MAVAKAANKG VDVTRHLVPK ARAASTAAVL VQTATRHGMP PGFKAKVGRL ETFTLPERVS
     GSVSDKAIAD AMIGAWRRDG ILQIGIYSGY IASGEEITDG IADYSEIFTV TKDLPHTDER
     VARGWPCHGP CPWLDQHMKA IMTRYMNDLA ESGEKLLQLI EMGLDIPTGS LTRYTNDGWH
     HMRVLRFPQN DRTNGKGKKG RGIGSHTDYG LLVIAAQDDV GGLFVRPPHE NERFSNWEKS
     SAGLRENEAG WVYVPPVAGT FTVFPGDMMQ YMTNNVLQST PHKVGLNVRE RFAFAYFHEP
     NFRSVIRPLP GHNAGQSPIE GIHYGTHFTN MFLRNYPDRV TTARLQEEGR YRLLESEELR
     DGDDVL
//